The ultimate aims of these studies continues to be to define the etiology, pathogenesis and treatment of amyloid disease. To accomplish this, we plan to define more precisely the biochemical and biophysical properties of amyloid fibril proteins and amyoid P-component; to study humoral and cellular immune function in patients with amyloid disease and to explore mechanisms of amyloid fibrillogenesis. The biochemical studies have been specifically designed to analyze and compare the primary structure of amyloid proteins of various origins (animal and human) and to determine the relation between tissue and serum amyloid precursors. Fibrillogenesis and reticuloendothelial cell function will be investigated using immunocytochemical autoradiographic and tissue culture techniques. We wish to test the hypothesis that primary, secondary and myeloma-associated amyloidosis share common pathogenic pathways, i.e. T (thymus) cell depletion, B (bursa-equivalent) cell activation and M (marrow) cell dysfunction and to attempt appropriate therapeutic intervention based on our findings in experimental animal models. We will examine the kinetics of the acute phase proteins, SAA and SAP as well as CRP while more precisely defining their role in the pathogenesis of amyloidosis.